Rubisco Assembly in the Chloroplast.
Rubisco Assembly in the Chloroplast.
复制标题
DOI：
10.3389/fmolb.2018.00024
复制
发表时间：
2018
影响因子：
5
通讯作者：
Feiz L
中科院分区：
文献类型：
--
作者：
Vitlin Gruber A;Feiz L
1,5-二磷酸核酮糖羧化酶/加氧酶 (Rubisco) 催化卡尔文-本森循环中的限速步骤，将大气中的碳转化为生物上有用的碳源。 Rubisco 的催化速率较慢且底物特异性较低，因此需要生产高水平的该酶。为了设计更高效的工厂 Rubisco，我们需要更好地了解它的折叠和组装过程。 I 型 Rubisco 存在于绿藻和维管植物中，是一种十六聚体，由叶绿体基因组编码的 8 个大亚基 (RbcL) 和 8 个核编码小亚基 (RbcS) 组成。与蓝藻同系物不同，蓝藻同系物可以在体外或在大肠杆菌中重建，并在细菌伴侣蛋白 (GroEL-GroES) 和 RbcX 伴侣的帮助下，功能性叶绿体 Rubisco 的生物发生需要 Cpn60-Cpn20、GroEL-GroES 的叶绿体同系物以及其他辅助因子，包括 Rubisco 积累因子 1 (Raf1)、Rubisco 积累因子 2 (Raf2) 和束鞘缺陷 2 (Bsd2)。这些因子的发现和表征为拟南芥 Rubisco 在大肠杆菌中的组装铺平了道路。在本综述中，我们讨论了异源寡聚伴侣蛋白复合物对 RbcL 折叠的独特性，以及后伴侣蛋白伴侣在全酶组装中的顺序或同时作用。每个组装因素发挥作用的确切阶段尚未确定。拟南芥 Rubisco 在大肠杆菌中的表达提供了一些关于 Raf1 和 RbcX 在促进 RbcL 寡聚化中的潜在作用、Bsd2 在全酶组装之前稳定寡聚核心以及 Raf2 在与 RbcL 和 RbcS 相互作用中的潜在作用的一些见解。从长远来看，每个已知因子的功能表征以及其他因子的潜在发现和表征将为设计更高效的植物奠定基础，具有更大的生物量，用于生物燃料和食物。
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step in the Calvin-Benson cycle, which transforms atmospheric carbon into a biologically useful carbon source. The slow catalytic rate of Rubisco and low substrate specificity necessitate the production of high levels of this enzyme. In order to engineer a more efficient plant Rubisco, we need to better understand its folding and assembly process. Form I Rubisco, found in green algae and vascular plants, is a hexadecamer composed of 8 large subunits (RbcL), encoded by the chloroplast genome and 8 small, nuclear-encoded subunits (RbcS). Unlike its cyanobacterial homolog, which can be reconstituted in vitro or in E. coli, assisted by bacterial chaperonins (GroEL-GroES) and the RbcX chaperone, biogenesis of functional chloroplast Rubisco requires Cpn60-Cpn20, the chloroplast homologs of GroEL-GroES, and additional auxiliary factors, including Rubisco accumulation factor 1 (Raf1), Rubisco accumulation factor 2 (Raf2) and Bundle sheath defective 2 (Bsd2). The discovery and characterization of these factors paved the way for Arabidopsis Rubisco assembly in E. coli. In the present review, we discuss the uniqueness of hetero-oligomeric chaperonin complex for RbcL folding, as well as the sequential or concurrent actions of the post-chaperonin chaperones in holoenzyme assembly. The exact stages at which each assembly factor functions are yet to be determined. Expression of Arabidopsis Rubisco in E. coli provided some insight regarding the potential roles for Raf1 and RbcX in facilitating RbcL oligomerization, for Bsd2 in stabilizing the oligomeric core prior to holoenzyme assembly, and for Raf2 in interacting with both RbcL and RbcS. In the long term, functional characterization of each known factor along with the potential discovery and characterization of additional factors will set the stage for designing more efficient plants, with a greater biomass, for use in biofuels and sustenance.
影响因子：
5
作者：
Vitlin Gruber A;Vugman M;Azem A;Weiss CE
通讯作者：
Weiss CE
影响因子：
3.7
作者：
Vitlin Gruber A;Nisemblat S;Zizelski G;Parnas A;Dzikowski R;Azem A;Weiss C
通讯作者：
Weiss C